Type
Text
Type
Thesis
Advisor
Karzai, Wali | Glynn, Steven
Date
2016-12-01
Keywords
Biochemistry
Department
Department of Biochemistry and Cell Biology
Language
en_US
Source
This work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.
Identifier
http://hdl.handle.net/11401/76891
Publisher
The Graduate School, Stony Brook University: Stony Brook, NY.
Format
application/pdf
Abstract
Abstract of the Thesis Replacement of Potassium Chloride by Potassium Glutamate Enhances the In Vitro Proteolytic Activity of Lon Protease By Poorna Kannan Master of Science In Biochemistry and Cell Biology Stony Brook University Critical for cell survival, protein quality control and protein turnover are orchestrated by AAA+ (ATPases associated with diverse cellular activities) proteases. In bacteria, Lon protease is one such ATP-dependent enzyme whose function, among others, includes degradation of misfolded proteins (1). In Yersinia pestis Lon protease is central to host invasion and pathogenicity. Among several substrates of Lon is the regulator of virulence A (RovA), a temperature-sensing protein in Yersinia (2). In this study, I have employed an in-vitro system to gain a better understanding of the proteolytic activity of Yersinia Lon. I show that while Lon is able to degrade RovA in the presence of potassium chloride, its proteolytic activity increases significantly when a more physiologically relevant salt, potassium glutamate, is used instead. | 22 pages
Recommended Citation
Kannan, Poorna, "Replacement of Potassium Chloride by Potassium Glutamate Enhances the In Vitro Proteolytic Activity of Lon Protease" (2016). Stony Brook Theses and Dissertations Collection, 2006-2020 (closed to submissions). 2765.
https://commons.library.stonybrook.edu/stony-brook-theses-and-dissertations-collection/2765